PXD013476 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Effects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry |
Description | Complex conformational dynamics are essential for the chaperone function of heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization establishing ATPase competence. Biochemical data demonstrate that the intrinsic, but weak, ATP hydrolyzing activity of Hsp90 is markedly enhanced by the co-chaperone Aha1. However, cellular concentration of Aha1 is substoichiometric relative to Hsp90. In cells, interaction of this important co-chaperone with Hsp90 is up-regulated by posttranslational modifications (PTMs), including phosphorylation of a highly conserved tyrosine (Y313 in Hsp90a). Here we use chemical cross-linking with mass spectrometry to explore the the impacts of a phosphomimetic mutation (Y313E) and binding of a non-hydrolyzable ATP analog (AMP-PNP),on the structure Hsp90a and its interaction with Aha1. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:55:17.485.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Juan Chavez |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ FT; Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-04-12 01:53:58 | ID requested | |
1 | 2019-06-17 03:21:48 | announced | |
⏵ 2 | 2024-10-22 04:55:22 | announced | 2024-10-22: Updated project metadata. |
Publication List
Xu W, Beebe K, Chavez JD, Boysen M, Lu Y, Zuehlke AD, Keramisanou D, Trepel JB, Prodromou C, Mayer MP, Bruce JE, Gelis I, Neckers L, Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1. Nat Commun, 10(1):2574(2019) [pubmed] |
10.1038/s41467-019-10463-y; |
Keyword List
submitter keyword: cross-linking, Aha1, PTM,heat shock, phosphorylation, XL-MS, chaperone, Hsp90 |
Contact List
Len Neckers |
contact affiliation | Urologic Oncology Branch, National Cancer Institute, Bethesda, MD 20892, USA |
contact email | neckersl@mail.nih.gov |
lab head | |
Juan Chavez |
contact affiliation | University of Washington |
contact email | jdchavez@uw.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD013476
- Label: PRIDE project
- Name: Effects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry